• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nature >X-ray structure of a calcium-activated TMEM16 lipid scramblase
【24h】

X-ray structure of a calcium-activated TMEM16 lipid scramblase

机译：钙激活的TMEM16脂质scramblase的X射线结构

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

在本期Nature上发表的两篇论文中，作者发布了两个由Ca~（2+）激发的氯化物通道的X-射线晶体结构，它们是这种类型通道的首次发表的结构。Janine Brunner等人使“脂质混杂酶”发生了结晶，这种酶是催化脂质在一个双层的两叶之间运动的一种膜蛋白。该结构显示了一个亲水性跨膜空腔，该空腔暴露于脂质双层，催化过程可能在那里发生。Veronica Dickson等人使“bestrophin-1”发生了结晶。这个家族的蛋白会响应于细胞内Ca~(2+)浓度的上升将它们的阴离子选择性小孔打开。该结构显示，Ca~(2+)结合到一个五聚跨膜通道的胞质区域；并且还显示，该小孔是95A长，有至少15个不同的阴离子结合点。%The TMEM16 family of proteins, also known as anoctamins, features a remarkable functional diversity. This family contains the long sought-after Ca~(2+)-activated chloride channels as well as lipid scramblases and cation channels. Here we present the crystal structure of a TMEM16 family member from the fungus Nectria haematococca that operates as a Ca~(2+)-activated lipid scramblase. Each subunit of the homodimeric protein contains ten transmembrane helices and a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer as a potential site of catalysis. This cavity harbours a conserved Ca~(2+) -binding site located within the hydrophobic core of the membrane. Mutations of residues involved in Ca~(2+) coordination affect both lipid scrambling in N. haematococca TMEM16 and ion conduction in the Cl~-channel TMEM16A. The structure reveals the general architecture of the family and its mode of Ca~(2+) activation. It also provides insight into potential scrambling mechanisms and serves as a framework to unravel the conduction of ions in certain TMEM16 proteins.
机译：在本期Nature上发表的两篇论文中，作者发布了两个由Ca~（2+）激发的氯化物通道的X-射线晶体结构，它们是这种类型通道的首次发表的结构。Janine Brunner等人使“脂质混杂酶”发生了结晶，这种酶是催化脂质在一个双层的两叶之间运动的一种膜蛋白。该结构显示了一个亲水性跨膜空腔，该空腔暴露于脂质双层，催化过程可能在那里发生。Veronica Dickson等人使“bestrophin-1”发生了结晶。这个家族的蛋白会响应于细胞内Ca~(2+)浓度的上升将它们的阴离子选择性小孔打开。该结构显示，Ca~(2+)结合到一个五聚跨膜通道的胞质区域；并且还显示，该小孔是95A长，有至少15个不同的阴离子结合点。%The TMEM16 family of proteins, also known as anoctamins, features a remarkable functional diversity. This family contains the long sought-after Ca~(2+)-activated chloride channels as well as lipid scramblases and cation channels. Here we present the crystal structure of a TMEM16 family member from the fungus Nectria haematococca that operates as a Ca~(2+)-activated lipid scramblase. Each subunit of the homodimeric protein contains ten transmembrane helices and a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer as a potential site of catalysis. This cavity harbours a conserved Ca~(2+) -binding site located within the hydrophobic core of the membrane. Mutations of residues involved in Ca~(2+) coordination affect both lipid scrambling in N. haematococca TMEM16 and ion conduction in the Cl~-channel TMEM16A. The structure reveals the general architecture of the family and its mode of Ca~(2+) activation. It also provides insight into potential scrambling mechanisms and serves as a framework to unravel the conduction of ions in certain TMEM16 proteins.

著录项

  • 来源
    《Nature》 |2014年第7530期|207-212a2|共7页
  • 作者

    Janine D. Brunner; Novandy K. Lim; Stephan Schenck; Alessia Duerst; Raimund Dutzler;

  • 作者单位

    Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland;

    Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland;

    Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland;

    Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland;

    Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号